› 1m4e

Solution NMR

Solution Structure of Hepcidin-20

Released:
DOI: 10.2210/pdb1m4e/pdb
PDB entry 1m4e coloured by chain, ensemble of 20 models, front view.
PDB entry 1m4e coloured by chain, ensemble of 20 models, side view.
PDB entry 1m4e coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis.
Hunter HN, Fulton DB, Ganz T, Vogel HJ
J Biol Chem 277 37597-603 (2002)
PMID: 12138110

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160483 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hepcidin-20 Chain: A
Molecule details ›
Chain: A
Length: 20 amino acids
Theoretical weight: 2.2 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P81172 (Residues: 65-84; Coverage: 33%)
Gene names: HAMP, HEPC, LEAP1, UNQ487/PRO1003
Sequence domains: Hepcidin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, molecular dynamics, matrix relaxation, torsion angle dynamics
Expression system: Not provided

Quick links

Citations

60 review citations

Anti-microbial peptides: from invertebrates to vertebrates.
Bulet et al. (2004)
59 more

1 mention without citation

Insights into the antimicrobial properties of hepcidins: advantages and drawbacks as potential therapeutic agents.
Lombardi et al. (2015)